Many consumer products, such as clothes and food packaging, are made of blends of polymers, long molecules consisting of repeating chemical units. The attractiveness of using blends of different polymers arises from the engineers’ desire to combine multiple unique properties of each individual polymer, such as transparency, stretchability, and breathability, into a seamless whole. However, different polymers are not necessarily miscible, a term scientists use to describe whether two materials mix at the molecular level. Miscibility isn’t a one-and-done kind of deal: scientists and engineers have known for years how to make polymer blends mix by careful temperature control. What if there were conditions other than temperature to achieve polymer blend miscibility? This may ultimately help in industrial processing of polymer blends. In this week’s paper, Professors Annika Kriisa and Connie B. Roth from Emory University in Atlanta, Georgia, explore the mixing dynamics of two polymers by using a strong electric field.
When an experiment doesn’t behave the way we expect, either our understanding of the relevant physics is flawed, or the phenomenon is more complicated than it appears. When a theoretical prediction is off by two orders of magnitude - like what was observed in this recent paper by Hua Yung Lo, Yuan Liu, and Lei Xu of the Chinese University of Hong Kong - something is seriously wrong.
Scientists often draw inspiration from biological organisms to describe phenomena, even when they are studying outside the realm of biology. Physicist Pierre-Gilles de Gennes was no exception. In 1971, after being inspired by the movement of snakes, he proposed reptation theory, or the reptation model, which has since been widely used to describe motions of polymers. As the name “reptation” suggests, de Gennes assumed polymer chains move like snakes. As shown in Figure 1, the model describes a polymer chain’s motion in an environment that is highly populated by other chains (shown in gray) by assuming that the chain is confined in a virtual tube (shown in red) formed by surrounding polymer chains. According to reptation theory, the chain wiggles through this tube, similar to a snake slithering through the woods. As one might imagine, directly imaging the snake-like slithering of polymers is a challenging affair; however, in today’s study, Maram Abadi and coworkers from King Abdullah University of Science and Technology were able to do just that with DNA chains – an example of a polymer – and compared their results to prevailing theory.
If you ever played tug-of-war in elementary school, you might remember that it isn’t the friendliest game. People fall over, hands get burned from holding on to the rope, and knees get scraped from falling on the ground. Although victory can be sweet, the injuries that come with it may make you never want to play the game again. Perhaps surprisingly, there is a similar ‘’tug-of-war” happening inside your body, as individual cells move around from one place to another in a process called cell migration. What’s more, this microscopic tug-of-war may help to heal those scrapes and bruises that happened in elementary school, and those that happen in your everyday life.
In my previous post on soft nanoparticles, you were introduced to polymer-based nanoparticles that could be used in biomedical applications, one of which is cancer therapy. These nanoparticles have a range of useful properties for cancer treatments, including their spherical shape and small size (~100 nm), both of which are similar to exosomes, small globules that are used in nature for transferring proteins between cells. Since cells naturally absorb exosomes, artificial particles with this size and shape should also be easy for cells to absorb, which means these particles could be used to deliver drugs into cells. While this idea sounds promising, it hasn’t worked out in practice -- when drug-loaded polymer-based nanoparticles were injected into a tumor, subsequent tests showed that less than 1% of the injected dose entered the cancer cells. Since these particles were the correct size and shape, why didn’t they get inside the target cells?
“USE YOUR LEGS!” That’s what might have been yelled at you the first time you went climbing. We are so used to walking or running that we don’t even think about how we do it. But when we face a new environment, such as a steep slope, we realize that finding the best strategy to move through space is not so easy. Now, imagine you are as small as few dozens of microns, without legs or arms, and you live in a viscous fluid. How would you move? This is the question biologists who are interested in cell movements have been trying to solve. By observing cells under a microscope, they saw that depending on their type or their environment, cells exhibit a wide variety of motion strategies. However, one thing never changes: cells need to exert forces on their environment to move. To do so, some kinds of cells create structures called focal adhesions. These structures are made up of several proteins, assembled on the outside of the cell. Like tiny bits of double-sided tape, their purpose is to stick the cell to whatever is nearby (see Figure 1). In slightly more technical language, focal adhesions connect the molecular skeleton of the cell to a substrate.
A honeybee colony can only exist when many individual bees cooperate. When a hive becomes too crowded, about 10,000 of the workers and a queen leave the hive to form their own colony. While the scout bees are searching for a new nest site, the rest of the bees are exposed to all of the dangers of the outside world, such as predators and storms, and have to stick together for protection. They form a “cluster”, which hangs on a nearby tree branch (as in Figure 1a) until a new suitable nest site is found. Sometimes, beekeepers hang these clusters from their faces as a “bee beard”.
For the most part of biology, it is form that follows function. Proteins are a perfect example of this -- they are made of a sequence of amino acids (the protein building units), which are synthesized by the ribosome. Once synthesized, the long strings of amino acids fold up into a particular 3D shape or conformational state. Proteins take less than a thousandth of a second to attain their preferred conformational state (called “native state”) that -- if nothing goes wrong -- ends up being the same for a given sequence. This process is called protein folding. Explaining how a protein finds its folding preference out of all possible ways in such a short time is a longstanding problem in biology.
We are surrounded by phenomena caused by the scattering of light. When enjoying a sunny day at the seaside, like in the photo at the top, why is the sky blue? Blue light scatters more than red light. Why is milk opaque? Protein and fat particles scatter light. If you are reading this with blue eyes, your eye color is due to light scattering. Scientists use the same general scattering principle to study the structure of soft materials using the scattering of well-defined radiation. Scattering measurements reveal structures between an ångström and hundreds of nanometers, an important region for studying soft matter. Just as the color of the sky results from light scattered by air molecules, the scattering of X-rays and neutrons tells us about the size and shape of compounds in soft materials along with their interactions, and I will focus on these two types of radiation.
Look inside a glass of milk. Still, smooth, and white. Now put a drop of that milk under a microscope. See? It’s not so smooth anymore. Fat globules and proteins dance around in random paths surrounded by water. Their dance—a type of movement called Brownian motion—is caused by collisions with water molecules that move around due to the thermal energy. This mixture of dancing particles in water is called a colloid.